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Conserved domains on  [gi|489930577|ref|WP_003833897|]
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MULTISPECIES: arabinose ABC transporter substrate-binding protein [Citrobacter]

Protein Classification

arabinose ABC transporter substrate-binding protein( domain architecture ID 10107481)

arabinose ABC transporter substrate-binding protein serves as the initial receptor in the high-affinity L-arabinose membrane transport system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 27-321 2.65e-141

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


:

Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 401.28  E-value: 2.65e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP-DGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYD 105
Cdd:cd01540    1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKmDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 106 MKVIAVDDQFANakGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGW-DVKSTAVMAITANELDTARRRTSGSMEALKA 184
Cdd:cd01540   81 IPVIAVDDQLVD--ADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKRGWdDVKEVGVLAITMDTLSVCVDRTDGAKDALKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 185 AGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKNWLIVGMNDNTVLGGVRATEGQGFKAPNVIGIGINGVDAVSELS 264
Cdd:cd01540  159 AGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWLVVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLAADEEF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489930577 265 KGEATGFYGSLLPSPDVHGYKSSEMLYNWVTKGAEPPAFTeVTDVVLITRDNFKEEL 321
Cdd:cd01540  239 KKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAET-LTDGVIVTRDNYKEVM 294
 
Name Accession Description Interval E-value
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 27-321 2.65e-141

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 401.28  E-value: 2.65e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP-DGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYD 105
Cdd:cd01540    1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKmDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 106 MKVIAVDDQFANakGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGW-DVKSTAVMAITANELDTARRRTSGSMEALKA 184
Cdd:cd01540   81 IPVIAVDDQLVD--ADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKRGWdDVKEVGVLAITMDTLSVCVDRTDGAKDALKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 185 AGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKNWLIVGMNDNTVLGGVRATEGQGFKAPNVIGIGINGVDAVSELS 264
Cdd:cd01540  159 AGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWLVVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLAADEEF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489930577 265 KGEATGFYGSLLPSPDVHGYKSSEMLYNWVTKGAEPPAFTeVTDVVLITRDNFKEEL 321
Cdd:cd01540  239 KKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAET-LTDGVIVTRDNYKEVM 294
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 27-320 1.98e-101

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 299.43  E-value: 1.98e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577   27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTL-NAIDSLAASGAKGFVICTPDPKlGPAIMAKARGYD 105
Cdd:pfam00532   3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLtNAIDLLLASGADGIIITTPAPS-GDDITAKAEGYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  106 MKVIAVDDQFANAkgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGwdvksTAVMAITANELdTARRRTSGSMEALKAA 185
Cdd:pfam00532  82 IPVIAADDAFDNP-----DGVPCVMPDDTQAGYESTQYLIAEGHKRP-----IAVMAGPASAL-TARERVQGFMAALAAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  186 GFPeKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQG-FKAPNVIGIGINGVDAVSELS 264
Cdd:pfam00532 151 GRE-VKIYHVATGDNDIPDAALAANAMLVSHPTID--AIVAMNDEAAMGAVRALLKQGrVKIPDIVGIGINSVVGFDGLS 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  265 KGEATGFYGSLLPSPDVH----GYKSSEMLYNWVtkgaepPAFTEVTDVVLITRDNFKEE 320
Cdd:pfam00532 228 KAQDTGLYLSPLTVIQLPrqllGIKASDMVYQWI------PKFREHPRVLLIPRDFFKET 281
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 18-316 1.97e-36

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 133.13  E-value: 1.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  18 SQSAIAESMKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVI-KIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGPA 96
Cdd:COG1879   26 AAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIvVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  97 IMAKARGYDMKVIAVDDQFANAKGkpmdtVPLVMMAATKIGERQGQELYKEMQKRGwdvksTAVMAITANELDTARRRTS 176
Cdd:COG1879  106 ALKKAKAAGIPVVTVDSDVDGSDR-----VAYVGSDNYAAGRLAAEYLAKALGGKG-----KVAILTGSPGAPAANERTD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 177 GSMEALKAagFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGING 256
Cdd:COG1879  176 GFKEALKE--YPGIKVVAEQYADWDREKALEVMEDLLQAHPDID--GIFAANDGMALGAAQALKAAG-RKGDVKVVGFDG 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489930577 257 V-DAVSELSKGEatgFYGSLLPSPDVHGYKSSEMLYNWVtKGAEPPAFTeVTDVVLITRDN 316
Cdd:COG1879  251 SpEALQAIKDGT---IDATVAQDPYLQGYLAVDAALKLL-KGKEVPKEI-LTPPVLVTKEN 306
 
Name Accession Description Interval E-value
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 27-321 2.65e-141

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 401.28  E-value: 2.65e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP-DGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYD 105
Cdd:cd01540    1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKmDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 106 MKVIAVDDQFANakGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGW-DVKSTAVMAITANELDTARRRTSGSMEALKA 184
Cdd:cd01540   81 IPVIAVDDQLVD--ADPMKIVPFVGIDAYKIGEAVGEWLAKEMKKRGWdDVKEVGVLAITMDTLSVCVDRTDGAKDALKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 185 AGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKNWLIVGMNDNTVLGGVRATEGQGFKAPNVIGIGINGVDAVSELS 264
Cdd:cd01540  159 AGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWLVVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLAADEEF 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489930577 265 KGEATGFYGSLLPSPDVHGYKSSEMLYNWVTKGAEPPAFTeVTDVVLITRDNFKEEL 321
Cdd:cd01540  239 KKQPTGFKASLYISPDKHGYIAAEELYNWITDGKPPPAET-LTDGVIVTRDNYKEVM 294
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 27-320 1.98e-101

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 299.43  E-value: 1.98e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577   27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTL-NAIDSLAASGAKGFVICTPDPKlGPAIMAKARGYD 105
Cdd:pfam00532   3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLtNAIDLLLASGADGIIITTPAPS-GDDITAKAEGYG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  106 MKVIAVDDQFANAkgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGwdvksTAVMAITANELdTARRRTSGSMEALKAA 185
Cdd:pfam00532  82 IPVIAADDAFDNP-----DGVPCVMPDDTQAGYESTQYLIAEGHKRP-----IAVMAGPASAL-TARERVQGFMAALAAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  186 GFPeKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQG-FKAPNVIGIGINGVDAVSELS 264
Cdd:pfam00532 151 GRE-VKIYHVATGDNDIPDAALAANAMLVSHPTID--AIVAMNDEAAMGAVRALLKQGrVKIPDIVGIGINSVVGFDGLS 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  265 KGEATGFYGSLLPSPDVH----GYKSSEMLYNWVtkgaepPAFTEVTDVVLITRDNFKEE 320
Cdd:pfam00532 228 KAQDTGLYLSPLTVIQLPrqllGIKASDMVYQWI------PKFREHPRVLLIPRDFFKET 281
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 18-316 1.97e-36

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 133.13  E-value: 1.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  18 SQSAIAESMKLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVI-KIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGPA 96
Cdd:COG1879   26 AAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIvVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  97 IMAKARGYDMKVIAVDDQFANAKGkpmdtVPLVMMAATKIGERQGQELYKEMQKRGwdvksTAVMAITANELDTARRRTS 176
Cdd:COG1879  106 ALKKAKAAGIPVVTVDSDVDGSDR-----VAYVGSDNYAAGRLAAEYLAKALGGKG-----KVAILTGSPGAPAANERTD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 177 GSMEALKAagFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGING 256
Cdd:COG1879  176 GFKEALKE--YPGIKVVAEQYADWDREKALEVMEDLLQAHPDID--GIFAANDGMALGAAQALKAAG-RKGDVKVVGFDG 250

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489930577 257 V-DAVSELSKGEatgFYGSLLPSPDVHGYKSSEMLYNWVtKGAEPPAFTeVTDVVLITRDN 316
Cdd:COG1879  251 SpEALQAIKDGT---IDATVAQDPYLQGYLAVDAALKLL-KGKEVPKEI-LTPPVLVTKEN 306
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 27-310 1.57e-31

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 118.82  E-value: 1.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEV-IKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYD 105
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELvVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 106 MKVIAVDDQFANAKgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkstAVMAITANEL-DTARRRTSGSMEALKA 184
Cdd:cd01536   81 IPVVAVDTDIDGGG----DVVAFVGTDNYEAGKLAGEYLAEALGGKG------KVAILEGPPGsSTAIDRTKGFKEALKK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 185 agFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGV-DAVSEL 263
Cdd:cd01536  151 --YPDIEIVAEQPANWDRAKALTVTENLLQANPDID--AVFAANDDMALGAAEALKAAG-RTGDIKIVGVDGTpEALKAI 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 489930577 264 SKGEatgFYGSLLPSPDVHGYKSSEMLYNWVtKGAEPPAFTEVTDVV 310
Cdd:cd01536  226 KDGE---LDATVAQDPYLQGYLAVEAAVKLL-NGEKVPKEILTPVTL 268
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 27-316 1.62e-21

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 92.04  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTL--NAIDsLAASGAKGFVICTPDPKLGPAIMAKARGY 104
Cdd:cd06319    1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQvtNAND-LIAQGVDGIIISPTNSSAAPTVLDLANEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 105 DMKVIaVDDQFANAKgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKSTAVMAITANElDTARRRTSGSMEALKA 184
Cdd:cd06319   80 KIPVV-IADIGTGGG----DYVSYIISDNYDGGYQAGEYLAEALKENGWGGGSVGIIAIPQSR-VNGQARTAGFEDALEE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 185 AGFPEKQIYQVPTKSNDipGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGVD-AVSEL 263
Cdd:cd06319  154 AGVEEVALRQTPNSTVE--ETYSAAQDLLAANPDIKG--IFAQNDQMAQGALQAIEEAG-RTGDILVVGFDGDPeALDLI 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489930577 264 SKGEATgfyGSLLPSPDVHGYKSSEMLYNWVtKGAEPPAFTEVTDVVLITRDN 316
Cdd:cd06319  229 KDGKLD---GTVAQQPFGMGARAVELAIQAL-NGDNTVEKEIYLPVLLVTSEN 277
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 29-292 8.65e-13

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 67.33  E-value: 8.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577   29 GFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI--AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYDM 106
Cdd:pfam13407   2 GVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgpAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  107 KVIAVDDQFANAKGkpmdtVPLVMMAATKIGERQGQELYKEMQKRGwdvkstAVMAITANELDT-ARRRTSGSMEALKaA 185
Cdd:pfam13407  82 PVVTFDSDAPSSPR-----LAYVGFDNEAAGEAAGELLAEALGGKG------KVAILSGSPGDPnANERIDGFKKVLK-E 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  186 GFPEKQIYQVPTKSNDIPG-AFDAANSMLVQHP-EVKnwLIVGMNDNTVLGGVRATEGQGFKA-PNVIGIGINGvDAVSE 262
Cdd:pfam13407 150 KYPGIKVVAEVEGTNWDPEkAQQQMEALLTAYPnPLD--GIISPNDGMAGGAAQALEAAGLAGkVVVTGFDATP-EALEA 226

                         250       260       270
                  ....*....|....*....|....*....|
gi 489930577  263 LSKGeatGFYGSLLPSPDVHGYKSSEMLYN 292
Cdd:pfam13407 227 IKDG---TIDATVLQDPYGQGYAAVELAAA 253
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 27-316 6.08e-12

periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380541 [Multi-domain]  Cd Length: 282  Bit Score: 65.12  E-value: 6.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYD 105
Cdd:cd06318    1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTdAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 106 MKVIAVDDQFaNAKGKPMDTvplVMMAATKIGERQGQELYKEMQKRgwDVKSTAVMAITANELDTARRrtSG-----SME 180
Cdd:cd06318   81 IPVITVDSAL-DPSANVATQ---VGRDNKQNGVLVGKEAAKALGGD--PGKIIELSGDKGNEVSRDRR--DGflagvNEY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 181 ALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIgigINGVDAV 260
Cdd:cd06318  153 QLRKYGKSNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDIN--VVYAENDDMALGAMKALKAAG-MLDKVK---VAGADGQ 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489930577 261 SELSKGEATGFYG-SLLPSPDVHGYKSSEMLYNWVTKGAEPPAFTEVTDvVLITRDN 316
Cdd:cd06318  227 KEALKLIKDGKYVaTGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPT-ALITKDN 282
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 38-313 1.38e-10

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 60.77  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  38 PWFQTEWKFADKAGKDLGFEViKIAVPDGEKTLNA----IDSLAASGAKGFVICTPDPK-LGPAImAKARGYDMKVIAVD 112
Cdd:cd06321   12 PFFVAMVRGAEEAAAEINPGA-KVTVVDARYDLAKqfsqIDDFIAQGVDLILLNAADSAgIEPAI-KRAKDAGIIVVAVD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 113 dqfANAKGkpMDTVplVMMAATKIGERQGQELYKEMQKRGwdvkstAVMAITANELDTARRRTSGSMEALKAagFPEKQI 192
Cdd:cd06321   90 ---VAAEG--ADAT--VTTDNVQAGYLACEYLVEQLGGKG------KVAIIDGPPVSAVIDRVNGCKEALAE--YPGIKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 193 YQVPTKSNDIPGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGFKapnviGIGINGVD----AVSELsKGEA 268
Cdd:cd06321  155 VDDQNGKGSRAGGLSVMTRMLTAHPDVDG--VFAINDPGAIGALLAAQQAGRD-----DIVITSVDgspeAVAAL-KREG 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489930577 269 TGFYGSLLPSPDVHGYKSSEMLYNwVTKGAEPPAFTEVTDVVLIT 313
Cdd:cd06321  227 SPFIATAAQDPYDMARKAVELALK-ILNGQEPAPELVLIPSTLVT 270
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 27-313 1.53e-10

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 60.71  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARG 103
Cdd:cd20008    1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPAteaDIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 104 yDMKVIAVDDQfANAKgkpmDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKSTAVMAITANElDTARRRTSGSMEALK 183
Cdd:cd20008   81 -GIPVVLVDSG-ANTD----DYDAFLATDNVAAGALAADELAELLKASGGGKGKVAIISFQAGS-QTLVDREEGFRDYIK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 184 AAgFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGVDAVSEL 263
Cdd:cd20008  154 EK-YPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVG--IFGANNPSAVGVAQALAEAG-KAGKIVLVGFDSSPDEVAL 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 489930577 264 SKGEATgfYGSLLPSPDVHGYKSSEMLYNwVTKGAEPPAFTEVTDVVLIT 313
Cdd:cd20008  230 LKSGVI--KALVVQDPYQMGYEGVKTAVK-ALKGEEIVEKNVDTGVTVVT 276
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 27-316 2.21e-10

periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 60.35  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVIcTP--DPKLGPAImAKA 101
Cdd:cd06320    1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPsetDTQGQLNLLETMLNKGYDAILV-SPisDTNLIPPI-EKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 102 RGYDMKVIAVDDQFANAKGKPM--DTVPLVMMAATKIGERQGQELYKEMQKRGwdvKSTAVMAITANEldTARRRTSGSM 179
Cdd:cd06320   79 NKKGIPVINLDDAVDADALKKAggKVTSFIGTDNVAAGALAAEYIAEKLPGGG---KVAIIEGLPGNA--AAEARTKGFK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 180 EALKAAgfPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGV-D 258
Cdd:cd06320  154 ETFKKA--PGLKLVASQPADWDRTKALDAATAILQAHPDLKG--IYAANDTMALGAVEAVKAAG-KTGKVLVVGTDGIpE 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489930577 259 AVSELSKGEATgfyGSLLPSPDVHGYKSSEMLYnWVTKGAEPPAFTeVTDVVLITRDN 316
Cdd:cd06320  229 AKKSIKAGELT---ATVAQYPYLEGAMAVEAAL-RLLQGQKVPAVV-ATPQALITKDN 281
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 27-313 1.19e-09

periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 58.08  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAImAKARGY 104
Cdd:cd06323    1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLdAQNDPAKQLSQVEDLIVRKVDALLINPTDSDaVSPAV-EEANEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 105 DMKVIAVDDQFANAKgkpmdTVPLVMMAATKIGERQGQELYKEMQKRGWDVKSTAVMAITAneldtARRRTSGSMEALKA 184
Cdd:cd06323   80 GIPVITVDRSVTGGK-----VVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSA-----ARERGKGFHNAIAK 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 185 agFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGFKapNVIGIGINGV-DAVSEL 263
Cdd:cd06323  150 --YPKINVVASQTADFDRTKGLNVMENLLQAHPDIDA--VFAHNDEMALGAIQALKAAGRK--DVIVVGFDGTpDAVKAV 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 489930577 264 SKGEatgFYGSLLPSPDVHGYKSSEMLYNWVtKGAEPPAFTEVtDVVLIT 313
Cdd:cd06323  224 KDGK---LAATVAQQPEEMGAKAVETADKYL-KGEKVPKKIPV-PLKLVT 268
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 65-306 1.44e-08

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 54.94  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  65 DGEKTLNAIDSLAASGAKGFVICTPDPKlGPAIMAKARGYDMKVIAVDdqFANAKGKPMDTvplVMMAATKIGERQGQEL 144
Cdd:cd01537   40 DQEKQNDQIDVLLAKRVKGLAINLVDPA-AAGVAEKARGQNVPVVFFD--KEPSRYDKAYY---VITDSKEGGIIQGDLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 145 YKEMQKRgwdvkstavMAITANELD--TARRRTSGSMEALKAAGFPEKQIyQVPTKSNDIPGAFDAANSMLVQhPEVKNW 222
Cdd:cd01537  114 AKHGHIQ---------IVLLKGPLGhpDAEARLAGVIKELNDKGIKTEQL-QLDTGDWDTASGKDKMDQWLSG-PNKPTA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 223 LIVGmNDNTVLGGVRATEGQGFKAPNviGIGINGVDAVSELSKgeATGFYGSLLPSPDVHGYKSSEMLYNWVTKGAEPPA 302
Cdd:cd01537  183 VIAN-NDAMAMGAVEALKEHGLRVPS--DISVFGYDALPEALK--SGPLLTTILQDANNLGKTTFDLLLNLADNWKIDNK 257


                 ....
gi 489930577 303 FTEV 306
Cdd:cd01537  258 VVRV 261
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 44-314 6.65e-08

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 53.01  E-value: 6.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  44 WKF----ADKAGKDLGFEVIKIAvPDGEKTLNA----IDSLAASGAKGFVIC-TPDPKLGPAImAKARGYDMKVIAVDdq 114
Cdd:cd20004   14 WKSvkagAEKAAQELGVEIYWRG-PSREDDVEAqiqiIEYFIDQGVDGIVLApLDRKALVAPV-ERARAQGIPVVIID-- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 115 fanakgKPMDTVPLVMMAAT---KIGERQGQELYKEMQKRGwdvksTAVMAITANELDTARRRTSGSMEALKaAGFPEKQ 191
Cdd:cd20004   90 ------SDLGGDAVISFVATdnyAAGRLAAKRMAKLLNGKG-----KVALLRLAKGSASTTDRERGFLEALK-KLAPGLK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 192 IYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGVDAVSE-LSKGEATG 270
Cdd:cd20004  158 VVDDQYAGGTVGEARSSAENLLNQYPDVD--GIFTPNESTTIGALRALRRLG-LAGKVKFIGFDASDLLLDaLRAGEISA 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489930577 271 FygsLLPSPDVHGYKSSEMLYNwVTKGAEPPAFTeVTDVVLITR 314
Cdd:cd20004  235 L---VVQDPYRMGYLGVKTAVA-ALRGKPVPKRI-DTGVVLVTK 273
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 27-323 1.26e-07

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 52.22  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVIcTP--DPKLGPAI-MAKAR 102
Cdd:cd06309    1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTdANQDQEKQINDIRDLIAQGVDAILI-SPidATGWDPVLkEAKDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 103 GydMKVIAVDDQFANAKGKpmDTVPLVMMAATKIGERQGQELYKEMQKrgwdvKSTAVMAITANE-LDTARRRTSGSMEA 181
Cdd:cd06309   80 G--IPVILVDRTIDGEDGS--LYVTFIGSDFVEEGRRAAEWLVKNYKG-----GKGNVVELQGTAgSSVAIDRSKGFREV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 182 LKAagFPEKQIyqVPTKSNDI--PGAFDAANSMLVQHPEVKNwLIVGMNDNTVLGGVRATEGQGFKAP-NVIGIGINGV- 257
Cdd:cd06309  151 IKK--HPNIKI--VASQSGNFtrEKGQKVMENLLQAGPGDID-VIYAHNDDMALGAIQALKEAGLKPGkDVLVVGIDGQk 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489930577 258 DAVSELSKGEATgfyGSLLPSPDvHGYKSSEMLYNWVtKGAEPPAFTEVTDVVlITRDNFKEELAK 323
Cdd:cd06309  226 DALEAIKAGELN---ATVECNPL-FGPTAFDTIAKLL-AGEKVPKLIIVEERL-FDKDNAAEELEP 285
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 27-259 1.60e-07

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 51.82  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVI-KIAVPDGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYD 105
Cdd:cd19992    1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIfQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 106 MKVIAVDDQFANAKgkpmdtVPL-VMMAATKIGERQGQELYKEMQKRGWdvkstAVMAITANElDTARRRTSGSMEALKA 184
Cdd:cd19992   81 VPVISYDRLILNAD------VDLyVGRDNYKVGQLQAEYALEAVPKGNY-----VILSGDPGD-NNAQLITAGAMDVLQP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 185 AGFPE--KQIYQVPTKsndipgAFDAANSMlvQHpeVKNWL---------IVGMNDNTVLGGVRATEGQGFkAPNVIgig 253
Cdd:cd19992  149 AIDSGdiKIVLDQYVK------GWSPDEAM--KL--VENALtannnnidaVLAPNDGMAGGAIQALKAQGL-AGKVF--- 214


                 ....*.
gi 489930577 254 INGVDA 259
Cdd:cd19992  215 VTGQDA 220
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 27-313 2.58e-07

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 51.04  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP--DGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGY 104
Cdd:cd06314    1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQksDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 105 DMKVIAVDDQFANAKGKpmdtvplvmmaaTKIG---ERQGQELYKEMQKRgwDVKSTAVMAITAN-ELDTARRRTSGSME 180
Cdd:cd06314   81 GIPVITFDSDAPDSKRL------------AYIGtdnYEAGREAGELMKKA--LPGGGKVAIITGGlGADNLNERIQGFKD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 181 ALKAAgfpeKQIYQVPTKSN--DIPGAFDAANSMLVQHPEVKNWLIVGMNDntVLGGVRATEGQG-FKAPNVIGIGINGv 257
Cdd:cd06314  147 ALKGS----PGIEIVDPLSDndDIAKAVQNVEDILKANPDLDAIFGVGAYN--GPAIAAALKDAGkVGKVKIVGFDTLP- 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489930577 258 DAVSELSKGEATGFYGSllpSPDVHGYKSSEMLYNWVTKGAEPPAFTEvTDVVLIT 313
Cdd:cd06314  220 ETLQGIKDGVIAATVGQ---RPYEMGYLSVKLLYKLLKGGKPVPDVID-TGVDVVT 271
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 32-313 4.43e-07

D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 50.40  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  32 VKQPEEPWFQTEWKFADKAGKDLGFEViKIAVPDGEKTLNA--IDSLAASGAKGfVICTP-DPKLGPAIMAKARGYDMKV 108
Cdd:cd19967    6 VSTPNNPFFVVEAEGAKEKAKELGYEV-TVFDHQNDTAKEAelFDTAIASGAKA-IILDPaDADASIAAVKKAKDAGIPV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 109 IAVDDQFaNAKGKPMDTVPLVMMAATKIGerqGQELYKEMQKRGWDVKstavmaITANELDT-ARRRTSGSMEALKaaGF 187
Cdd:cd19967   84 FLIDREI-NAEGVAVAQIVSDNYQGAVLL---AQYFVKLMGEKGLYVE------LLGKESDTnAQLRSQGFHSVID--QY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 188 PEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGING----VDAVSEl 263
Cdd:cd19967  152 PELKMVAQQSADWDRTEAFEKMESILQANPDIK--GVICGNDEMALGAIAALKAAG-RAGDVIIVGFDGsndvRDAIKE- 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489930577 264 SKGEATGfygslLPSPDVHGYKSSEMLYNWVTKGAepPAFTEV--TDVVLIT 313
Cdd:cd19967  228 GKISATV-----LQPAKLIARLAVEQADQYLKGGS--TGKEEKqlFDCVLIT 272
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 35-262 4.81e-07

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 50.68  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  35 PEEPWFQTEWKFADKAGKDLGFEV-IKIAVPDGEKTLNAIDSLAASGAK-GFVICTPDPKLGPAIMAKARGYDMKVIAVD 112
Cdd:cd06324   10 EDEPFWQNVTRFMQAAAKDLGIELeVLYANRNRFKMLELAEELLARPPKpDYLILVNEKGVAPELLELAEQAKIPVFLIN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 113 DQFANAK----GKPMDT--------VPlvmmAATKIGERQGQELYKEMQKRGWDVKSTaVMAITANELDTA-RRRTSGSM 179
Cdd:cd06324   90 NDLTDEErallGKPREKfkywlgsiVP----DNEQAGYLLAKALIKAARKKSDDGKIR-VLAISGDKSTPAsILREQGLR 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 180 EALKAAgfPEKQIYQVptksndIPG------AFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGFKA-PNVIgi 252
Cdd:cd06324  165 DALAEH--PDVTLLQI------VYAnwsedeAYQKTEKLLQRYPDID--IVWAANDAMALGAIDALEEAGLKPgKDVL-- 232

                        250
                 ....*....|
gi 489930577 253 gINGVDAVSE 262
Cdd:cd06324  233 -VGGIDWSPE 241
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 27-315 6.53e-07

periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380525 [Multi-domain]  Cd Length: 296  Bit Score: 49.93  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIA--VPDGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAIMaKARG 103
Cdd:cd06302    1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGptQADAAQQVQIVENLIAQGVDAIAVSPNDADaLAPVLK-KAKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 104 YDMKVIAVDDQfANAKGKPMDtvplVMMAATKIgerQGQELYKEMQKRgwdVKSTAVMAITANELDTARRRT-SGSMEAL 182
Cdd:cd06302   80 AGIKVITWDSD-APPSARDYF----VNQADDEG---LGEALVDSLAKE---IGGKGKVAILSGSLTATNLNAwIKAMKEY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 183 KAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGVDAVSE 262
Cdd:cd06302  149 LKSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAYPDLK--GIIGVSTTAPPAAAQAVEEAG-KTGKVAVTGIGLPNTARP 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489930577 263 LSK-GEATGFYgslLPSPDVHGYKSSEMLYNWVTKGAEPPAFTEVTDVVLITRD 315
Cdd:cd06302  226 YLKdGSVKEGV---LWDPAKLGYLTVYAAYQLLKGKGFTEDSDDVGTGGKVKVD 276
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 47-315 9.57e-07

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 49.55  E-value: 9.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  47 ADKAGKDLGFEVIKIAvPDGE----KTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYDMKVIAVDdqfanaKGKP 122
Cdd:cd20005   21 AEQAAKELGVKITFEG-PDTEsdvdKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFD------SGVP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 123 MDTVplVMMAAT---KIGERQGQELYKEMQKRGwdvkSTAVMAITANELdTARRRTSGSMEALKAAgFPEKQIYQVPTKS 199
Cdd:cd20005   94 SDLP--LATVATdnyAAGALAADHLAELIGGKG----KVAIVAHDATSE-TGIDRRDGFKDEIKEK-YPDIKVVNVQYGV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 200 NDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGVDAVSELSKGEAtgFYGSLLPSP 279
Cdd:cd20005  166 GDHAKAADIAKAILQANPDLK--GIYATNEGAAIGVANALKEMG-KLGKIKVVGFDSGEAQIDAIKNGV--IAGSVTQNP 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 489930577 280 DVHGYKSSEMLYNwVTKGAEPPAFTEvTDVVLITRD 315
Cdd:cd20005  241 YGMGYKTVKAAVK-ALKGEEVEKLID-TGAKWYDKD 274
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 49-283 1.09e-06

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 49.20  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  49 KAGKDLGFEVIkIAVPDGE--KTLNAIDSLAASGAKGFVICTPDPK-LGPAIMAkARGYDMKVIAVDdqfANAKGkpmDT 125
Cdd:cd06322   23 KEAAELGVKVV-VADANGDlaKQLSQIEDFIQQGVDAIILAPVDSGgIVPAIEA-ANEAGIPVFTVD---VKADG---AK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 126 VplvmmaATKIGERQ---GQELYKEMQKRGWDVKSTAVMaITANELDTARRRTSGSMEALKAAgfPEKQIYQVPTKSNDI 202
Cdd:cd06322   95 V------VTHVGTDNyagGKLAGEYALKALLGGGGKIAI-IDYPEVESVVLRVNGFKEAIKKY--PNIEIVAEQPGDGRR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 203 PGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGINGVD-AVSELSKGEAtgFYGSLLPSPDV 281
Cdd:cd06322  166 EEALAATEDMLQANPDLD--GIFAIGDPAALGALTAIESAG-KEDKIKVIGFDGNPeAIKAIAKGGK--IKADIAQQPDK 240


                 ..
gi 489930577 282 HG 283
Cdd:cd06322  241 IG 242
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 27-300 3.95e-06

periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 47.38  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGfevIKIAVPDGE----KTLNAIDSLAASGAKGFVICTPDPK-LGPAIMAKA 101
Cdd:cd19968    1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLG---VKLVVLDAQnsssKQASDLENAIAQGVDGIIVSPIDVKaLVPAIEAAI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 102 RGyDMKVIAVDdqfANAKGKPMdtVPLVMMAATKIGERQGQELYKEMQKRGWDVKSTAVMAITaneldTARRRTSGSMEA 181
Cdd:cd19968   78 KA-GIPVVTVD---RRAEGAAP--VPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSS-----PAIDRTKGFHEE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 182 LKAAgfPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKNwLIVGMNDNTVLGGVRATEGQGFKAPNVIGIGINGV-DAV 260
Cdd:cd19968  147 LAAG--PKIKVVFEQTGNFERDEGLTVMENILTSLPGPPD-AIICANDDMALGAIEAMRAAGLDLKKVKVIGFDAVpDAL 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489930577 261 SELSKGEAtgfYGSLLPSPDVHGYKSSEMLYNWVTKGAEP 300
Cdd:cd19968  224 QAIKDGEL---YATVEQPPGGQARTALRILVDYLKDKKAP 260
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 65-259 5.34e-06

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 47.28  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  65 DGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYDMKVIAVDdqfANAKGKPMD---TVPLVmmaatKIGERQG 141
Cdd:cd19995   43 DASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYD---RLILGGPADyyvSFDNV-----AVGEAQA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 142 QELYKEMqkRGWDVKSTAVMAITANELDT-ARRRTSGSMEALKAAGFPE--KQIYQVPTKSNDIPGAFDAANSMLVQHPE 218
Cdd:cd19995  115 QSLVDHL--KAIGKKGVNIVMINGSPTDNnAGLFKKGAHEVLDPLGDSGelKLVCEYDTPDWDPANAQTAMEQALTKLGN 192

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489930577 219 vKNWLIVGMNDNTVLGGVRATEGQGFKAPNVIGiginGVDA 259
Cdd:cd19995  193 -NIDGVLSANDGLAGGAIAALKAQGLAGKVPVT----GQDA 228
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 27-265 8.01e-06

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 46.47  E-value: 8.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGK-DLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAImAKA 101
Cdd:cd19970    1 KVALVMKSLANEFFIEMEKGARKHAKeANGYELLVKGIKqetDIEQQIAIVENLIAQKVDAIVIAPADSKaLVPVL-KKA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 102 RGYDMKVI----AVDDQFANAKGKPmdtVPLVMMAATKIGERQGQELYKEMQKRGwdvkstAVMAITAN-ELDTARRRTS 176
Cdd:cd19970   80 VDAGIAVInidnRLDADALKEGGIN---VPFVGPDNRQGAYLAGDYLAKKLGKGG------KVAIIEGIpGADNAQQRKA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 177 GSMEALKAAGFpekQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGfKAPNVIGIGING 256
Cdd:cd19970  151 GFLKAFEEAGM---KIVASQSANWEIDEANTVAANLLTAHPDIR--GILCANDNMALGAIKAVDAAG-KAGKVLVVGFDN 224


                 ....*....
gi 489930577 257 VDAVSELSK 265
Cdd:cd19970  225 IPAVRPLLK 233
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 49-292 2.27e-05

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 45.27  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  49 KAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAIMAkARGYDMKVIAVDDQFANAkgKPMDTV 126
Cdd:cd19971   23 KAVEANGDELITRdPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEgIRPALEA-AKEAGIPVINVDTPVKDT--DLVDST 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 127 plVMMAATKIGERQGQELYKEMQKRGwdvkstAVMAITANELDTARRRTSGSMEALKA-AGFpeKQIYQVPTKSnDIPGA 205
Cdd:cd19971  100 --IASDNYNAGKLCGEDMVKKLPEGA------KIAVLDHPTAESCVDRIDGFLDAIKKnPKF--EVVAQQDGKG-QLEVA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 206 FDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGqgfkAPNVIGIGINGVDAVSELSKG-EATGFYGSLLPSPDVHGY 284
Cdd:cd19971  169 MPIMEDILQAHPDLD--AVFALNDPSALGALAALKA----AGKLGDILVYGVDGSPDAKAAiKDGKMTATAAQSPIEIGK 242


                 ....*...
gi 489930577 285 KSSEMLYN 292
Cdd:cd19971  243 KAVETAYK 250
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 29-126 5.62e-05

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380628 [Multi-domain]  Cd Length: 285  Bit Score: 44.00  E-value: 5.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  29 GFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVP---DGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAImAKARGY 104
Cdd:cd19973    3 GLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKidgDNATQVTAIENMIAAGAKGILITPSDTKaIVPAV-KKARDA 81

                         90       100
                 ....*....|....*....|..
gi 489930577 105 DMKVIAVDDQFanakgKPMDTV 126
Cdd:cd19973   82 GVLVIALDTPT-----DPIDAA 98
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 169-251 5.80e-05

ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 44.12  E-value: 5.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 169 DTARRRTSGSMEALKAAGFPEKQIYQVPTKSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGFKAPN 248
Cdd:cd06279  146 SVARERLAGYRDALEEAGLDLDDVPVVEAPGNTEEAGRAAARALLALDPRPT--AILCMSDVLALGALRAARERGLRVPE 223


                 ....*.
gi 489930577 249 ---VIG 251
Cdd:cd06279  224 dlsVTG 229
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 27-316 7.28e-05

periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 43.80  E-value: 7.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVK-QPEEpwFQTEWKFADKA-GKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAImAKAR 102
Cdd:cd06313    1 KIGFTVYgLSSE--FITNLVEAMKAvAKELNVDLVVLdGNGDVSTQINQVDTLIAQGVDAIIVVPVDADaLAPAV-EKAK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 103 GYDMKVIAVddqfaNAKGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVKSTAVMAITAnELDtarrRTSGSMEAL 182
Cdd:cd06313   78 EAGIPLVGV-----NALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSA-QID----RGKGIENVL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 183 KaagfpekqiyqvptKSNDI------PGAFDAANSMLVqhpeVKNWL---------IVGMNDNTVLGGVRATEGQGFKap 247
Cdd:cd06313  148 K--------------KYPDIkvlaeqTANWSRDEAMSL----MENWLqaygdeidgIIAQNDDMALGALQAVKAAGRD-- 207

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 248 NVIGIGINGV-DAVSELSKGEatgFYGSLLPSPDVHGYKSSEMLYNWVTKGAEPPafTEVTDVVLITRDN 316
Cdd:cd06313  208 DIPVVGIDGIeDALQAVKSGE---LIATVLQDAEAQGKGAVEVAVDAVKGEGVEK--KYYIPFVLVTKDN 272
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 47-313 8.99e-05

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 43.48  E-value: 8.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  47 ADKAGKDLGFEVIKIAvPDGEKTLNA----IDSLAASGAKGFVICTPDPKLGPAIMAKARGYDMKVIAVDdqfanAKGKP 122
Cdd:cd06310   21 AEAAAKDLGVKIIFVG-PESEEDVAGqnslLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVID-----SGIKG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 123 MDTVPLVMMAATKIGERQGQELYKEMQKRGwdvkSTAVMAITANElDTARRRTSGSMEALKAAGfPEKQIYQVPTKSNDI 202
Cdd:cd06310   95 DAYLSYIATDNYAAGRLAAQKLAEALGGKG----KVAVLSLTAGN-STTDQREEGFKEYLKKHP-GGIKVLASQYAGSDY 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 203 PGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGFKAPnvigIGINGVDAVSELSKG-EATGFYGSLLPSPDV 281
Cdd:cd06310  169 AKAANETEDLLGKYPDIDG--IFATNEITALGAAVAIKSRKLSGQ----IKIVGFDSQEELLDAlKNGKIDALVVQNPYE 242

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489930577 282 HGYKSSEMLYNwVTKGAEPPAFTEvTDVVLIT 313
Cdd:cd06310  243 IGYEGIKLALK-LLKGEEVPKNID-TGAELIT 272
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 36-220 1.46e-04

monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 42.64  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  36 EEPWFQTEWKFADKAGKDLGFEVIKIAVPDG--EKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYDMKVIAVDd 113
Cdd:cd19965   10 TNPFFQPVKKGMDDACELLGAECQFTGPQTFdvAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFN- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 114 qfANAKGKPMDTVPLVMMAATKIGERQGQELYKEMQKRGWDVkstaVMAITANELDTARRRTSGSMEALKAAGFPEKqiY 193
Cdd:cd19965   89 --VDAPGGENARLAFVGQDLYPAGYVLGKRIAEKFKPGGGHV----LLGISTPGQSALEQRLDGIKQALKEYGRGIT--Y 160

                        170       180
                 ....*....|....*....|....*..
gi 489930577 194 QVPTKSNDIPGAFDAANSMLVQHPEVK 220
Cdd:cd19965  161 DVIDTGTDLAEALSRIEAYYTAHPDIK 187
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
 28-252 2.34e-04

ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 42.25  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  28 LGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIkIAV----PDGEKTLnaIDSLAASGAKGfVICTPDPKLGPAIMaKARG 103
Cdd:cd06280    2 IGLIVPDITNPFFTTIARGIEDAAEKHGYQVI-LANtdedPEKEKRY--LDSLLSKQVDG-IILAPSAGPSRELK-RLLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 104 YDMKVIAVDDQFANAKgkpmdtVPLVMMAATKIGERQGQELYKEMQKRgwdvkstaVMAITAN-ELDTARRRTSGSMEAL 182
Cdd:cd06280   77 HGIPIVLIDREVEGLE------LDLVAGDNREGAYKAVKHLIELGHRR--------IGLITGPlEISTTRERLAGYREAL 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 183 KAAGFPEKQIYqVPTKSNDIPGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGFKAPNVIGI 252
Cdd:cd06280  143 AEAGIPVDESL-IFEGDSTIEGGYEAVKALLDLPPRPTA--IFATNNLMAVGALRALRERGLEIPQDISV 209
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
25-251 3.60e-04

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 41.72  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  25 SMKLGFLVKQPEEPWF-------QTEwkfADKAGKDLgfeVIKIAVPDGEKTLNAIDSLAASGAKGFVICTPDpkLGPAI 97
Cdd:COG1609   61 TRTIGVVVPDLSNPFFaellrgiEEA---ARERGYQL---LLANSDEDPEREREALRLLLSRRVDGLILAGSR--LDDAR 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  98 MAKARGYDMKVIAVDDQFANAKgkpmdtVPLVMMAATKIGERQGQELYKemqkRGWdvksTAVMAITANE-LDTARRRTS 176
Cdd:COG1609  133 LERLAEAGIPVVLIDRPLPDPG------VPSVGVDNRAGARLATEHLIE----LGH----RRIAFIGGPAdSSSARERLA 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489930577 177 GSMEALKAAGFPEKQIYQVPTkSNDIPGAFDAANSMLVQHPEVKnwLIVGMNDNTVLGGVRATEGQGFKAPN---VIG 251
Cdd:COG1609  199 GYREALAEAGLPPDPELVVEG-DFSAESGYEAARRLLARGPRPT--AIFCANDLMALGALRALREAGLRVPEdvsVVG 273
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 65-301 4.61e-04

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 41.42  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  65 DGEKTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGYDMKVIavddqFANAkgKPMDtvpLVMMAATKI-------- 136
Cdd:cd01539   42 DQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVI-----FFNR--EPSR---EDLKSYDKAyyvgtdae 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 137 --GERQGQELYKEMQK-RGWD-----VKSTAVMAITANELDTArRRTSGSMEALKAAGFPEKQIyqvptksndipgAFDA 208
Cdd:cd01539  112 esGIMQGEIIADYWKAnPEIDkngdgKIQYVMLKGEPGHQDAI-ARTKYSVKTLNDAGIKTEQL------------AEDT 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 209 ANSMLVQHPE-VKNWL---------IVGMNDNTVLGGVRATEGQGF------KAPNVIGI-GINgvDAVSELSKGEAtgf 271
Cdd:cd01539  179 ANWDRAQAKDkMDAWLskygdkielVIANNDDMALGAIEALKAAGYntgdgdKYIPVFGVdATP--EALEAIKEGKM--- 253

                        250       260       270
                 ....*....|....*....|....*....|
gi 489930577 272 YGSLLPSPDVHGYKSSEMLYNwVTKGAEPP 301
Cdd:cd01539  254 LGTVLNDAKAQAKAIYELAKN-LANGKEPL 282
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 35-262 7.98e-04

monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 40.39  E-value: 7.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  35 PEEPWFQTEWKFADKAGKDLGFEViKIAVPDG--EKTLNAIDSLAASGAKGFVICT--PDPKLGPAI-MAKARGydMKVI 109
Cdd:cd19966   10 PGDPFWTVVYNGAKDAAADLGVDL-DYVFSSWdpEKMVEQFKEAIAAKPDGIAIMGhpGDGAYTPLIeAAKKAG--IIVT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 110 AVD-DQFANAKGKPMDTVplvmmaatkIG---ERQGQELYKEMQKRGwDVKS--TAVMAITANELDTARRRTSGSMEALK 183
Cdd:cd19966   87 SFNtDLPKLEYGDCGLGY---------VGadlYAAGYTLAKELVKRG-GLKTgdRVFVPGLLPGQPYRVLRTKGVIDALK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 184 AAGFpekqIYQVPTKSNDIPGAFDAANSM---LVQHPEVKnwLIVGMNDNTVLGGVRATEGQGFKAPNVIGIGI----NG 256
Cdd:cd19966  157 EAGI----KVDYLEISLEPNKPAEGIPVMtgyLAANPDVK--AIVGDGGGLTANVAKYLKAAGKKPGEIPVAGFdlspAT 230


                 ....*.
gi 489930577 257 VDAVSE 262
Cdd:cd19966  231 VQAIKS 236
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 27-152 8.77e-04

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380657  Cd Length: 295  Bit Score: 40.38  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGE--KTLNAIDSLAASGAKGFVICTPDPKLGPAIMAKARGY 104
Cdd:cd20002    1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGPADADpaQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489930577 105 DMKVIAvdDQFANAKGKPMDtvpLVMMAATKIGERQGQELYKEMQKRG 152
Cdd:cd20002   81 GIVVIT--HESPGQKGADWD---VELIDNEKFGEAQMELLAKEMGGKG 123
PBP1_ABC_unchar_transporter cd06325
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems ...
 27-118 1.42e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally.


Pssm-ID: 380548  Cd Length: 282  Bit Score: 39.79  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVkQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTLNAIDSLAASGAKGFVIcTPDPKLG---PAIMAKARG 103
Cdd:cd06325  133 RVGVLY-NPGEPNSVAQLEELEAAAKKLGLELVEVPVSSPADIEQAFASLAGKVADALYV-PTDNTVAsarPRIAALALK 210

                         90
                 ....*....|....*
gi 489930577 104 YDMKVIAVDDQFANA 118
Cdd:cd06325  211 ARIPVIYSDREFVEA 225
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 40-270 1.77e-03

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 39.38  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  40 FQTE-WKFAD----KAGKDLGFEVIKI-AVPDGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAImAKARGYDMKVIAVD 112
Cdd:cd19993    9 FQEErWKTDEaamkKALEKAGAKYISAdAQSSAEKQLDDIESLISQGAKALIVLAQDGDaILPAV-EKAAAEGIPVIAYD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 113 dqfanakgKPMDT--VPLVMMAATKIGERQGQELYKEmqkrgwdVKSTAVMAITANELDT-ARRRTSGSMEALKAA---- 185
Cdd:cd19993   88 --------RLIENpiAFYISFDNVEVGRMQARGVLKA-------KPEGNYVFIKGSPTDPnADFLRAGQMEVLQPAidsg 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 186 -----------GF-PE---KQIYQVPTKSNDipgAFDAansmlvqhpevknwlIVGMNDNTVLGGVRATEGQGFKApnvi 250
Cdd:cd19993  153 kikivgeqytdGWkPAnaqKNMEQILTANNN---KVDA---------------VVASNDGTAGGAVAALAAQGLAG---- 210

                        250       260
                 ....*....|....*....|....
gi 489930577 251 GIGINGVD----AVSELSKGEATG 270
Cdd:cd19993  211 KVPVSGQDadkaALNRIALGTQTV 234
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 27-113 2.49e-03

rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380655  Cd Length: 298  Bit Score: 39.16  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIA--VPDGEKTLNAIDSLAASGAKGFVICTPDP-KLGPAiMAKARG 103
Cdd:cd20000    1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGptTATAEAQIPFINTLIQQGVDAIAISANDPdALAPA-LKKARA 79

                         90
                 ....*....|
gi 489930577 104 YDMKVIAVDD 113
Cdd:cd20000   80 AGIKVVTFDS 89
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 27-313 2.62e-03

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 38.76  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  27 KLGFLVKQPEEPWFQTEWKFADKAGKDLGFEVIKIAVPDGEKTL--NAIDSLAASGAKGFVICTPDPKLGPAIMAKARGY 104
Cdd:cd20007    1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLqtPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 105 DMKVIAVdDQFANAKGkpmdtvplvmMAATKI-------GERQGQELYKEMQKRGwdvkSTAVMAITANELDTARRRTsG 177
Cdd:cd20007   81 GIKVVTV-DTTLGDPS----------FVLSQIasdnvagGALAAEALAELIGGKG----KVLVINSTPGVSTTDARVK-G 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577 178 SMEALKAAGfpekQIYQVPTK--SNDIPGAFDAANSMLVQHPEVKNwlIVGMNDNTVLGGVRATEGQGfKAPNVIGIGIN 255
Cdd:cd20007  145 FAEEMKKYP----GIKVLGVQysENDPAKAASIVAAALQANPDLAG--IFGTNTFSAEGAAAALRNAG-KTGKVKVVGFD 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489930577 256 GVDA-VSELSKGEatgFYGSLLPSPDVHGYKSSEMLYNWVTkGAEPPAFTeVTDVVLIT 313
Cdd:cd20007  218 ASPAqVEQLKAGT---IDALIAQKPAEIGYLAVEQAVAALT-GKPVPKDI-LTPFVVIT 271
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 34-144 9.15e-03

periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 37.22  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489930577  34 QPEEPWFQTEwKFADKAGKDLGFEV-IKIAVPDGEKTLNAIDSLAASGAKGFVICTPDPK-LGPAImAKARGYDMKVIAV 111
Cdd:cd19994    9 KSEERWIKDG-ENLKSELEEAGYTVdLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSaLGDVL-EEAKDAGIPVIAY 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489930577 112 DDQfanakgkPMDTvPLVMMAAT----KIGERQGQEL 144
Cdd:cd19994   87 DRL-------IMNT-DAVDYYVTfdneKVGELQGQYL 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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